6ZU5

Structure of the Paranosema locustae ribosome in complex with Lso2

これはPDB形式変換不可エントリーです。

6ZU5 の概要

• エントリーDOI: 10.2210/pdb6zu5/pdb
• EMDBエントリー: 11437
• 分子名称: 25S rRNA, eL31, eL6, ... (77 entities in total)
• 機能のキーワード: microsporidia, pathogen, ribosome, hibernation, genome compaction
• 由来する生物種: Paranosema locustae; 詳細
• タンパク質・核酸の鎖数: 74
• 化学式量合計: 2628109.12

構造登録者

Ehrenbolger, K.,Jespersen, N.,Sharma, H.,Sokolova, Y.Y.,Tokarev, Y.S.,Vossbrinck, C.R.,Barandun, J. (登録日: 2020-07-21, 公開日: 2020-11-04, 最終更新日: 2024-05-01)

主引用文献

Ehrenbolger, K.,Jespersen, N.,Sharma, H.,Sokolova, Y.Y.,Tokarev, Y.S.,Vossbrinck, C.R.,Barandun, J.
Differences in structure and hibernation mechanism highlight diversification of the microsporidian ribosome.
Plos Biol., 18:e3000958-e3000958, 2020

PubMed Abstract: Assembling and powering ribosomes are energy-intensive processes requiring fine-tuned cellular control mechanisms. In organisms operating under strict nutrient limitations, such as pathogenic microsporidia, conservation of energy via ribosomal hibernation and recycling is critical. The mechanisms by which hibernation is achieved in microsporidia, however, remain poorly understood. Here, we present the cryo-electron microscopy structure of the ribosome from Paranosema locustae spores, bound by the conserved eukaryotic hibernation and recycling factor Lso2. The microsporidian Lso2 homolog adopts a V-shaped conformation to bridge the mRNA decoding site and the large subunit tRNA binding sites, providing a reversible ribosome inactivation mechanism. Although microsporidian ribosomes are highly compacted, the P. locustae ribosome retains several rRNA segments absent in other microsporidia, and represents an intermediate state of rRNA reduction. In one case, the near complete reduction of an expansion segment has resulted in a single bound nucleotide, which may act as an architectural co-factor to stabilize a protein-protein interface. The presented structure highlights the reductive evolution in these emerging pathogens and sheds light on a conserved mechanism for eukaryotic ribosome hibernation.

PubMed: 33125369
DOI: 10.1371/journal.pbio.3000958

実験手法

ELECTRON MICROSCOPY (2.9 Å)